The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26

Autores
Harries, Eleonora del Milagro; Gandía, Mónica; Carmona, Lourdes; Marcos, José F.
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The activity of protein O-mannosyltransferases (Pmt) affects the morphogenesis and virulence of fungal pathogens. PMT genes have been recently shown to determine the sensitivity of Saccharomyces cerevisiae to the antifungal peptide PAF26. This study reports the identification and characterisation of the three Pdpmt genes in the citrus postharvest pathogen Penicillium digitatum. The Pdpmt genes are expressed during fungal growth and fruit infection, with the highest induction for Pdpmt2. Pdpmt2 complemented the growth defect of the S. cerevisiae Δpmt2 strain. The Pdpmt2 gene mutation in P. digitatum caused pleiotropic effects, including the reduction of fungal growth and virulence, while its constitutive expression had no phenotypic effect. The Pdpmt2 null mutants also showed a distinctive colourless phenotype with a strong reduction in the number of conidia, which was associated with severe alterations in the development of conidiophores. Additional effects of the Pdpmt2 mutation were hyphal morphological alterations, increased sensitivity to cell wall-interfering compounds, and a blockage of invasive growth. In contrast,the Pdpmt2 mutation increased tolerance to oxidative stress and to the antifungal activity of PAF26. These data confirm the role of protein O-glycosylation in the PAF26-mediated antifungal mechanism present in distant fungal species. Important to future crop protection strategies, this study demonstrates that a mutation rendering fungi more resistant to an antifungal peptide results in severe deleterious effects on fungal growth and virulence.
Fil: Harries, Eleonora del Milagro. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta; Argentina
Fil: Gandía, Mónica. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España
Fil: Carmona, Lourdes. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España
Fil: Marcos, José F.. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España
Materia
Penicillium
Glycosylation
Mannosyltransferase
Virulence
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/7105
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/7105
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26Harries, Eleonora del MilagroGandía, MónicaCarmona, LourdesMarcos, José F.PenicilliumGlycosylationMannosyltransferaseVirulencehttps://purl.org/becyt/ford/4.4https://purl.org/becyt/ford/4The activity of protein O-mannosyltransferases (Pmt) affects the morphogenesis and virulence of fungal pathogens. PMT genes have been recently shown to determine the sensitivity of Saccharomyces cerevisiae to the antifungal peptide PAF26. This study reports the identification and characterisation of the three Pdpmt genes in the citrus postharvest pathogen Penicillium digitatum. The Pdpmt genes are expressed during fungal growth and fruit infection, with the highest induction for Pdpmt2. Pdpmt2 complemented the growth defect of the S. cerevisiae Δpmt2 strain. The Pdpmt2 gene mutation in P. digitatum caused pleiotropic effects, including the reduction of fungal growth and virulence, while its constitutive expression had no phenotypic effect. The Pdpmt2 null mutants also showed a distinctive colourless phenotype with a strong reduction in the number of conidia, which was associated with severe alterations in the development of conidiophores. Additional effects of the Pdpmt2 mutation were hyphal morphological alterations, increased sensitivity to cell wall-interfering compounds, and a blockage of invasive growth. In contrast,the Pdpmt2 mutation increased tolerance to oxidative stress and to the antifungal activity of PAF26. These data confirm the role of protein O-glycosylation in the PAF26-mediated antifungal mechanism present in distant fungal species. Important to future crop protection strategies, this study demonstrates that a mutation rendering fungi more resistant to an antifungal peptide results in severe deleterious effects on fungal growth and virulence.Fil: Harries, Eleonora del Milagro. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta; ArgentinaFil: Gandía, Mónica. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; EspañaFil: Carmona, Lourdes. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; EspañaFil: Marcos, José F.. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; EspañaWiley2015-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/7105Harries, Eleonora del Milagro; Gandía, Mónica; Carmona, Lourdes; Marcos, José F.; The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26; Wiley; Molecular Plant Pathology; 16; 7; 1-2015; 748–7611464-6722enginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/mpp.12232/abstractinfo:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/altIdentifier/doi/10.1111/mpp.12232info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:26:13Zoai:ri.conicet.gov.ar:11336/7105instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:26:14.006CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26
title The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26
spellingShingle The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26
Harries, Eleonora del Milagro
Penicillium
Glycosylation
Mannosyltransferase
Virulence
title_short The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26
title_full The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26
title_fullStr The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26
title_full_unstemmed The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26
title_sort The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26
dc.creator.none.fl_str_mv Harries, Eleonora del Milagro
Gandía, Mónica
Carmona, Lourdes
Marcos, José F.
author Harries, Eleonora del Milagro
author_facet Harries, Eleonora del Milagro
Gandía, Mónica
Carmona, Lourdes
Marcos, José F.
author_role author
author2 Gandía, Mónica
Carmona, Lourdes
Marcos, José F.
author2_role author
author
author
dc.subject.none.fl_str_mv Penicillium
Glycosylation
Mannosyltransferase
Virulence
topic Penicillium
Glycosylation
Mannosyltransferase
Virulence
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.4
https://purl.org/becyt/ford/4
dc.description.none.fl_txt_mv The activity of protein O-mannosyltransferases (Pmt) affects the morphogenesis and virulence of fungal pathogens. PMT genes have been recently shown to determine the sensitivity of Saccharomyces cerevisiae to the antifungal peptide PAF26. This study reports the identification and characterisation of the three Pdpmt genes in the citrus postharvest pathogen Penicillium digitatum. The Pdpmt genes are expressed during fungal growth and fruit infection, with the highest induction for Pdpmt2. Pdpmt2 complemented the growth defect of the S. cerevisiae Δpmt2 strain. The Pdpmt2 gene mutation in P. digitatum caused pleiotropic effects, including the reduction of fungal growth and virulence, while its constitutive expression had no phenotypic effect. The Pdpmt2 null mutants also showed a distinctive colourless phenotype with a strong reduction in the number of conidia, which was associated with severe alterations in the development of conidiophores. Additional effects of the Pdpmt2 mutation were hyphal morphological alterations, increased sensitivity to cell wall-interfering compounds, and a blockage of invasive growth. In contrast,the Pdpmt2 mutation increased tolerance to oxidative stress and to the antifungal activity of PAF26. These data confirm the role of protein O-glycosylation in the PAF26-mediated antifungal mechanism present in distant fungal species. Important to future crop protection strategies, this study demonstrates that a mutation rendering fungi more resistant to an antifungal peptide results in severe deleterious effects on fungal growth and virulence.
Fil: Harries, Eleonora del Milagro. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta; Argentina
Fil: Gandía, Mónica. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España
Fil: Carmona, Lourdes. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España
Fil: Marcos, José F.. Consejo Superior de Investigaciones Cientificas. Instituto de Agroquimica y Tecnologia de Alimentos; España
description The activity of protein O-mannosyltransferases (Pmt) affects the morphogenesis and virulence of fungal pathogens. PMT genes have been recently shown to determine the sensitivity of Saccharomyces cerevisiae to the antifungal peptide PAF26. This study reports the identification and characterisation of the three Pdpmt genes in the citrus postharvest pathogen Penicillium digitatum. The Pdpmt genes are expressed during fungal growth and fruit infection, with the highest induction for Pdpmt2. Pdpmt2 complemented the growth defect of the S. cerevisiae Δpmt2 strain. The Pdpmt2 gene mutation in P. digitatum caused pleiotropic effects, including the reduction of fungal growth and virulence, while its constitutive expression had no phenotypic effect. The Pdpmt2 null mutants also showed a distinctive colourless phenotype with a strong reduction in the number of conidia, which was associated with severe alterations in the development of conidiophores. Additional effects of the Pdpmt2 mutation were hyphal morphological alterations, increased sensitivity to cell wall-interfering compounds, and a blockage of invasive growth. In contrast,the Pdpmt2 mutation increased tolerance to oxidative stress and to the antifungal activity of PAF26. These data confirm the role of protein O-glycosylation in the PAF26-mediated antifungal mechanism present in distant fungal species. Important to future crop protection strategies, this study demonstrates that a mutation rendering fungi more resistant to an antifungal peptide results in severe deleterious effects on fungal growth and virulence.
publishDate 2015
dc.date.none.fl_str_mv 2015-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/7105
Harries, Eleonora del Milagro; Gandía, Mónica; Carmona, Lourdes; Marcos, José F.; The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26; Wiley; Molecular Plant Pathology; 16; 7; 1-2015; 748–761
1464-6722
url http://hdl.handle.net/11336/7105
identifier_str_mv Harries, Eleonora del Milagro; Gandía, Mónica; Carmona, Lourdes; Marcos, José F.; The Penicillium digitatum protein O Mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26; Wiley; Molecular Plant Pathology; 16; 7; 1-2015; 748–761
1464-6722
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/mpp.12232/abstract
info:eu-repo/semantics/altIdentifier/doi/
info:eu-repo/semantics/altIdentifier/doi/10.1111/mpp.12232
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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